Affiliation:
1. Department of Biochemistry, University of Birmingham, Birmingham B15 2TT, U.K.
Abstract
1. On electrophoresis in dissociating conditions the tropomyosins isolated from skeletal muscles of mammalian, avian and amphibian species migrated as two components. These were comparable with the α and β subunits of tropomyosin present in rabbit skeletal muscle. 2. The α and β components of all skeletal-muscle tropomyosins contained 1 and 2 residues of cysteine per 34000g respectively. 3. The ratio of the amounts of α and β subunit present in skeletal muscle tropomyosins was characteristic for the muscle type. Muscle consisting of slow red fibres contained a greater proportion of β-tropomyosin than muscles consisting predominantly of white fast fibres. 4. Mammalian and avian cardiac muscle tropomyosins consisted of α-tropomyosin only. 5. Mammalian and avian smooth-muscle tropomyosins differed both chemically and immunologically from striated-muscle tropomyosins. 6. Antibody raised against rabbit skeletal α-tropomyosin was species non-specific, reacting with all other striated muscle α-tropomyosin subunits tested. 7. Antibody raised against rabbit skeletal β-tropomyosin subunit was species-specific.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
226 articles.
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